title: Isolation and characterization of a soluble, immunoactive peptide of glial fibrillary acidic protein.
abstract: A soluble immunoactive peptide with a molecular weight of 16 000 was isolated and purified from the cyanogen bromide digest of the insoluble 50 000 dalton glial fibrillary acidic protein by Sephacryl S-200 gel filtration followed by DEAE-Bio-gel A chromatography. The homogeneity of the peptide was established by SDS-polyacrylamide gel electrohporesis and isoelectric focusing. The peptide from several species showed immunocrossreaction with rabbit antibody to intact glial fibrillary acidic protein. The peptide has a pI value of 5.32. The amino acid sequence of 28 residues from the amino terminus of the calf peptide has been determined.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D005904:Glial Fibrillary Acidic Protein; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000032:analysis*; D010446:Peptide Fragments / Q000302:isolation & purification*; D013045:Species Specificity
chemical_list: D000596:Amino Acids; D005904:Glial Fibrillary Acidic Protein; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D003488:Cyanogen Bromide